The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Heat‐Shock Proteins
Abstract
Heat‐shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell‐cycle control and signaling, and protection of cells against stress/apoptosis. More recently, HSPs have been implicated in antigen presentation with the role of chaperoning and transferring antigenic peptides to the class I and class II molecules of the major histocompatibility complexes. In addition, extracellular HSPs can stimulate professional antigen‐presenting cells of the immune system, such as macrophages and dendritic cells. HSPs constitute a large family of proteins that are often classified based on their molecular weight: hsp10, hsp40, hsp60, hsp70, hsp90, etc. This unit contains a table that lists common HSPs and summarizes their characteristics including (a) name, (b) subcellular localization, (c) known function, (d) chromosome assignment, (e) brief comments, and (f) references.
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Citations
Cites
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Roles of heat-shock proteins in innate and adaptive immunity.
Srivastava, P. (2002) · Nature reviews. Immunology · doi:10.1038/nri749 · Cited by 1,069
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Metadata
- Authors
- Li, Z., & Srivastava, P.
- Venue
- Current Protocols in Immunology
- Publisher
- Wiley
- Published
- 2003-12
- Volume
- 58
- Issue
- 1
- Pages
- Appendix 1T-Appendix 1T
- ISSN
- 1934-3671 (ISSN-L)
- 1934-368X
- OpenAlex
- W2766889331
- Cited by
- 285
- References
- 2
- FWCI
- 0.75
- Type
- journal article
- Language
- en
- Open access
- closed
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